Linked Life Data

20521994

Source:http://linkedlifedata.com/resource/pubmed/id/20521994

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-6-24
pubmed:abstractText
Receptor protein tyrosine phosphatases (RPTPs) have cell adhesion molecule-like extracellular domains coupled to cytoplasmic tyrosine phosphatase domains. PTPmu is the prototypical member of the type IIb subfamily of RPTPs, which includes PTPrho, PTPkappa, and PCP-2. The authors performed the first comprehensive analysis of the subfamily in one system, examining adhesion and antibody recognition. The authors evaluated if antibodies that they developed to detect PTPmu also recognized other subfamily members. Notably, each antibody recognizes distinct subsets of type IIb RPTPs. PTPmu, PTPrho, and PTPkappa have all been shown to mediate cell-cell aggregation, and prior work with PCP-2 indicated that it can mediate bead aggregation in vitro. This study reveals that PCP-2 is unique among the type IIb RPTPs in that it does not mediate cell-cell aggregation via homophilic binding. The authors conclude from these experiments that PCP-2 is likely to have a distinct biological function other than cell-cell aggregation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1543-5180
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34-47
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Characterization of the adhesive properties of the type IIb subfamily receptor protein tyrosine phosphatases.
pubmed:affiliation
Department of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, Ohio, USA.
pubmed:publicationType
Journal Article